| pubmed-article:7490292 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7490292 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:7490292 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:7490292 | lifeskim:mentions | umls-concept:C0292221 | lld:lifeskim |
| pubmed-article:7490292 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7490292 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:7490292 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:7490292 | pubmed:dateCreated | 1996-1-2 | lld:pubmed |
| pubmed-article:7490292 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7490292 | pubmed:abstractText | The Saccharomyces cerevisiae EMP47 gene encodes a nonessential type-I transmembrane protein with sequence homology to a class of intracellular lectins defined by ERGIC-53 and VIP36. The 12-amino acid COOH-terminal cytoplasmic tail of Emp47p ends in the sequence KTKLL, which conforms with the consensus for di-lysine-based ER-localization signals. Despite the presence of this motif, Emp47p was shown to be a Golgi protein at steady-state. The di-lysine motif of Emp47p was functional when transplanted onto Ste2p, a plasma membrane protein, conferring ER localization. Nevertheless, the di-lysine motif was required for Golgi-localization of Emp47p and showed the same charge-independent, position-dependent characteristics of other di-lysine motifs. Alpha-COP has been shown to be required for ER localization of di-lysine-tagged proteins. Consistent with this finding, the Ste2p-Emp47p hybrid protein was mislocalized to the cell surface in the alpha-COP mutant, ret1-1. Surprisingly, the Golgi-localization of Emp47p was unaffected by the ret1-1 mutation. To investigate whether Emp47p undergoes retrograde transport from the Golgi to the ER like other di-lysine-tagged proteins we developed an assay to measure this step after block of forward transport in a sec12 mutant. Under these conditions retrograde transport led to a specific redistribution of Emp47p from the Golgi to the ER. This recycling occurred from a Golgi subcompartment containing alpha 1,3 mannose-modified oligosaccharides suggesting that it originated from a medial-or later Golgi compartment. Thus Emp47p cycles between the Golgi apparatus and the ER and requires a di-lysine motif for its alpha-COP-independent, steady state localization in the Golgi. | lld:pubmed |
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| pubmed-article:7490292 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7490292 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7490292 | pubmed:citationSubset | IM | lld:pubmed |
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